Mechanistic studies on the reactions of bacterial methionine .gamma.-lyase with olefinic amino acids

Biochemistry ◽  
1981 ◽  
Vol 20 (15) ◽  
pp. 4325-4333 ◽  
Author(s):  
Michael Johnston ◽  
Ronald Raines ◽  
Michael Chang ◽  
Nobuyoshi Esaki ◽  
Kenji Soda ◽  
...  
Keyword(s):  
Amino Acids ◽  
Mechanistic Studies ◽  
Methionine Gamma Lyase

N-bromosuccinimide oxidation of dipeptides and their amino acids: Synthesis, kinetics and mechanistic studies

2006 ◽  
Vol 38 (6) ◽  
pp. 376-385 ◽  
Author(s):  
N. S. Linge Gowda ◽  
M. N. Kumara ◽  
D. Channe Gowda ◽  
K. S. Rangappa
Keyword(s):  
Amino Acids ◽  
Mechanistic Studies

scholarly journals 1.12 Å resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2

2017 ◽  
Vol 73 (8) ◽  
pp. 443-449 ◽  
Author(s):  
Katie Coates ◽  
Timothy R. Walsh ◽  
James Spencer ◽  
Philip Hinchliffe
Keyword(s):  
Crystal Structure ◽  
Amino Acids ◽  
High Resolution ◽  
Active Site ◽  
Catalytic Domain ◽  
Resistance Determinant ◽  
Mechanistic Studies ◽  
Colistin Resistance ◽  
Gram Negative ◽  
Starting Model

MCR-2 confers resistance to colistin, a `last-line' antibiotic against extensively resistant Gram-negative pathogens. It is a plasmid-encoded phosphoethanolamine transferase that is closely related to MCR-1. To understand the diversity in the MCR family, the 1.12 Å resolution crystal structure of the catalytic domain of MCR-2 was determined. Variable amino acids are located distant from both the di-zinc active site and the membrane-proximal face. The exceptionally high resolution will provide an accurate starting model for further mechanistic studies.

scholarly journals Diastereoselective Synthesis of b-Branched a-Amino Acids via Bio-catalytic Dynamic Kinetic Resolution

2021 ◽  
Author(s):  
Fuzhuo Li ◽  
Li-Cheng Yang ◽  
Jingyang Zhang ◽  
Jason Chen ◽  
Hans Renata
Keyword(s):  
Amino Acids ◽  
Total Synthesis ◽  
Kinetic Resolution ◽  
Diastereoselective Synthesis ◽  
Mechanistic Studies ◽  
Dynamic Kinetic Resolution ◽  
Resolution Process ◽  
Biocatalytic Reaction

We report a biocatalytic transamination method to prepare a broad range of b-branched a-amino acids that proceeds with high diastereo- and enantioselectivity. Mechanistic studies show that the transformation proceeds through a dynamic kinetic resolution process that is unique to the optimal enzyme. To highlight its utility and practicality, the biocatalytic reaction is applied to the synthesis of several cyclic fragments and in the first total synthesis of jomthonic acid A.

scholarly journals Structure of the methanofuran/methanopterin-biosynthetic enzyme MJ1099 fromMethanocaldococcus jannaschii

2014 ◽  
Vol 70 (11) ◽  
pp. 1472-1479 ◽  
Author(s):  
Thomas A. Bobik ◽  
Erick J. Morales ◽  
Annie Shin ◽  
Duilio Cascio ◽  
Michael R. Sawaya ◽  
...  
Keyword(s):  
Amino Acids ◽  
Greenhouse Gas ◽  
Active Site ◽  
Methanogenic Archaea ◽  
Anomalous Scattering ◽  
Biosynthetic Enzyme ◽  
Mechanistic Studies ◽  
Methanocaldococcus Jannaschii ◽  
C1 Metabolism ◽  
Tim Barrel

Prior studies have indicated that MJ1099 fromMethanocaldococcus jannaschiihas roles in the biosynthesis of tetrahydromethanopterin and methanofuran, two key cofactors of one-carbon (C1) metabolism in diverse organisms including the methanogenic archaea. Here, the structure of MJ1099 has been solved to 1.7 Å resolution using anomalous scattering methods. The results indicate that MJ1099 is a member of the TIM-barrel superfamily and that it is a homohexamer. Bioinformatic analyses identified a potential active site that is highly conserved among MJ1099 homologs and the key amino acids involved were identified. The results presented here should guide further studies of MJ1099 including mechanistic studies and possibly the development of inhibitors that target the methanogenic archaea in the digestive tracts of humans and that are a source of the greenhouse gas methane.

scholarly journals Mechanistic studies of the immunochemical termination of self-tolerance with unnatural amino acids

2009 ◽  
Vol 106 (11) ◽  
pp. 4337-4342 ◽  
Author(s):  
J. Grunewald ◽  
G. S. Hunt ◽  
L. Dong ◽  
F. Niessen ◽  
B. G. Wen ◽  
...  
Keyword(s):  
Amino Acids ◽  
Unnatural Amino Acids ◽  
Mechanistic Studies ◽  
Self Tolerance

Oxidation of the Natural Amino Acids by a Ferryl Complex: Kinetic and Mechanistic Studies with Peptide Model Compounds

2009 ◽  
Vol 48 (16) ◽  
pp. 7729-7739 ◽  
Author(s):  
Ahmed I. Abouelatta ◽  
Ashley A. Campanali ◽  
Anil R. Ekkati ◽  
Mark Shamoun ◽  
Suneth Kalapugama ◽  
...  
Keyword(s):  
Amino Acids ◽  
Mechanistic Studies ◽  
Model Compounds ◽  
Natural Amino Acids

β-Cyclodextrin catalyzed oxidation of some α-amino acids with chloramine-T in alkaline medium: Kinetics and mechanistic studies

2012 ◽  
Vol 353-354 ◽  
pp. 111-116 ◽  
Author(s):  
P.A. Prasantha ◽  
N.C. Sandhya ◽  
B.K. Kempegowda ◽  
D.G. Bhadregowda ◽  
K. Mantelingu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Alkaline Medium ◽  
Mechanistic Studies ◽  
Chloramine T ◽  
Catalyzed Oxidation

scholarly journals Molecular Engineering of Pediocin A to Establish Structure/Function Relationships for Mechanistic Control of Foodborne Pathogens

1993 ◽  
Author(s):  
Thomas J. Montville ◽  
Roni Shapira
Keyword(s):  
Amino Acids ◽  
Structure Function ◽  
Foodborne Pathogens ◽  
Structural Model ◽  
Consensus Sequence ◽  
Molecular Engineering ◽  
Atp Depletion ◽  
Mechanistic Studies ◽  
Antimicrobial Function ◽  
Genetically Determined

This project relates the structure of the bacteriocin molecule (which is genetically determined) to its antimicrobial function. We have sequenced the 19,542 bp pediocin plasmid pMD136 and developed a genetic transfer system for pediococci. The pediocin A operon is complex, containing putative structural, immunity, processing, and transport genes. The deduced sequence of the pediocin A molecule contains 44 amino acids and has a predicted PI of 9.45. Mechanistic studies compared the interaction of pediocin PA-1 and nisin with Listeria monocytgenes cells and model lipid systems. While significant nisin-induced intracellular ATP depletion is caused by efflux, pediocin-induced depletion is caused exclusively by hydrolysis. Liposomes derived from L. monocytogenes phospholipids were used to study the physical chemistry of pediocin and nisin interactions with lipids. Their different pH optima are the results of different specific ionizable amino acids. We generated a predicted 3-D structural model for pediocin PA-1 and used a variety of mutant pediocins to demonstrate that the "positive patch" at residues 11 and 12 (and not the YGNGV consensus sequence) is responsible for the binding step of pediocin action. This structure/function understanding gained here provides necessary prerequisites to the more efficacious use of bacteriocins to control foodborne pathogens.

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